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Multi-user quipament approved in grant 2014/17264-3: 2D nanoUPLC system

Grant number: 17/14476-8
Support type:Multi-user Equipment Program
Duration: August 01, 2017 - July 31, 2024
Field of knowledge:Biological Sciences - Biochemistry - Chemistry of Macromolecules
Principal researcher:Fabio Cesar Gozzo
Grantee:Fabio Cesar Gozzo
Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:14/17264-3 - New frontiers in structural proteomics: characterizing protein and protein complex structures by mass spectrometry, AP.TEM
As informações de acesso ao Equipamento Multiusuário são de responsabilidade do Pesquisador responsável
EMU web page: Página do Equipamento Multiusuário não informada
Type of equipment:Caracterização de Materiais - Análises Químicas - Cromatrografia líquida
Manufacturer: Fabricante não informado
Model: nanoUPLC 2D


The study of protein interactions is an important field to understand protein functions. This is, however, one area of great experimental difficulties due to inherent complexity of proteins and peptides. High resolution structural tools (i.e. X-Ray diffraction and Nuclear Magnetic Resonance are the de facto methods for these studies. However, most proteins and protein complexes are not amenable to have their structures solved by these techniques, requiring the use of other alternative methods to structurally characterize proteins and proteins complexes. Mass Spectrometry (MS) is an attractive technique for characterization of proteins due to its intrinsic characteristics, such as sensitivity, speed and broad applicability. Our group have been working on this field in the last 6 years (MS (da Silva et al, 2013, Fioramonte et al., 2012; Santos et al., 2011a; Santos et al., 2011b; Santos et al., 2010; Iglesias et al., 2010; Iglesias et al., 2009). In this project, we intend to use MS to characterize the structure of proteins and protein complexes. These experiments will be performed to obtain distance constrains from cross-linking experiments along with data from hydrogen/deuterium experiments and ion mobility and all these data will be used in a combined fashion to generate structural models of protein and complexes of biological interest. (AU)